SDA chemical crosslinking mass spectrometry was used to investigate the interaction between the Cds1 kinase and Ca2+-Calmodulin from Schizosaccharomyces pombe. Upon binding of Ca2+-Calmodulin, Cds1 is allosterically inhibited.
Recombinant proteins were mixed and then crosslinked either with DMTMM or by SDA and UV exposure. Complexes were resolved by SDS-PAGE, excised and tryptic peptides identified by MS.
